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Glycobiology Advance Access published online on August 29, 2006
Glycobiology, doi:10.1093/glycob/cwl041
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received May 12, 2006
Revised August 16, 2006
Accepted August 27, 2006

Article

Characterization of a carbohydrate epitope defined by the monoclonal antibody H185: Sialic acid O-acetylation on epithelial cell surface mucins

Pablo Argüeso 1 * and Mika Sumiyoshi 1

1 Schepens Eye Research Institute and Department of Ophthalmology, Harvard Medical School, 20 Staniford St., Boston, MA 02114-2508, USA

* To whom correspondence should be addressed.
Pablo Argüeso, E-mail: argueso{at}vision.eri.harvard.edu


  Abstract

Sialic acids comprise a large family of derivatives of neuraminic acid containing methyl, acetyl, sulfate and phosphate among other groups, which confer specific physicochemical properties (e.g., hydrophobicity, resistance to hydrolases) to the molecules carrying them. Several years ago a monoclonal antibody, designated H185, was developed, which binds to cell membranes of human corneal, conjunctival, laryngeal, and vaginal epithelia, and whose distribution is altered on the ocular surface of patients with keratinizing disease. Recent findings using immunoprecipitation and immunodepletion techniques have demonstrated that, in human corneal epithelial cells, the H185 antigen is carried by the membrane-associated mucin MUC16. In this study, we show that the H185 epitope on human corneal cells and in tear fluid is an O-acetylated sialic acid epitope that can be selectively hydrolyzed in an enzyme concentration-dependent manner by sialidase from A. ureafaciens, and to a lesser extent by sialidases from Newcastle disease virus, C. perfringens, and S. pneumoniae. Binding of the H185 antibody was impaired by treatment of tear fluid with a recombinant 9-O-acetylesterase from influenza C virus. Two O-acetyl derivatives, Neu5,7Ac2 and Neu5,9Ac2, were identified in human tear fluid by fluorometric HPLC and electrospray mass spectrometry. Immunoprecipitation of the H185 epitope from human corneal epithelial cells revealed that Neu5,9Ac2 was the major derivative on the mucin isolate. These results indicate that exposed wet-surfaced epithelia are decorated with O-acetyl sialic acid derivatives on membrane-associated mucins and suggest that O-acetylation on cell surfaces may protect against pathogen infection by preventing degradation of membraneassociated mucins.

Keywords: cell surface mucin/corneal epithelium/H185 antibody/MUC16/O-acetyl sialic acid.
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